References of "Zoli, André Pagnah"
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See detailMolécules de la famille des protéases aspartiques dans le placenta des ruminants: hormones ou protéines ?
Beckers, Jean-François ULg; Roberts, R. Michael; Zoli, André Pagnah et al

in Bulletin et Mémoires de l'Académie Royale de Médecine de Belgique (1994), 149(8-11), 355-367

The placenta of ruminant contains binucleate trophoblastic cells synthesizing proteins, migrating cross the barrier and fusing with endothelial cells of the endometrium. Recently described were two ... [more ▼]

The placenta of ruminant contains binucleate trophoblastic cells synthesizing proteins, migrating cross the barrier and fusing with endothelial cells of the endometrium. Recently described were two glycoproteins from the family of aspartic proteases, apparently lacking the enzymatic activity: the pregnancy associated glycorproteins I and II (PAGI and PAGII). The first (PAGI) is largely secreted in maternal blood, this characteristic copes with the lack of proteolytic activity. The second (PAGII) is not completely characterized. However, it binds to lutropin (LH) receptors with high affinity. This binding allows to assume that PAGII is likely the same as the bovine chorionic gonadotropin identified earlier (bCG). A better characterization of these glycoproteins (PAGI and PAGII) and other members of the family (PAGIII...) will answer these questions together with the unexplained invasive process of the placenta. [less ▲]

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See detailRadioimmunoassay of a Bovine Pregnancy-Associated Glycoprotein in Serum: Its Application for Pregnancy Diagnosis
Zoli, André Pagnah; Guilbault, Louis A; Delahaut, Philippe et al

in Biology of Reproduction (1992), 46(1), 83-92

A sensitive and specific double-antibody RIA for a bovine pregnancy-associated glycoprotein (bPAG) is described. The limit of detection was 0.2 ng/ml. The assay was specific for bPAG in that pituitary and ... [more ▼]

A sensitive and specific double-antibody RIA for a bovine pregnancy-associated glycoprotein (bPAG) is described. The limit of detection was 0.2 ng/ml. The assay was specific for bPAG in that pituitary and placental gonadotropic hormones and other placental or serum proteins assayed in serial dilutions did not cross-react. The RIA allowed measurement of bPAG in placental extracts, fetal serum, fetal fluids, and serum or plasma of pregnant cows. About 20% of unbred heifers and nonpregnant cows had detectable levels ranging from 0.30 +/- 0.09 to 0.50 +/- 0.17 ng/ml (mean +/- SD), and 15% of bull sera showed higher concentrations (3.01 +/- 1.73 ng/ml) of bPAG or bPAG-like protein. Variations among animals was observed in fetal serum bPAG concentrations. Bovine PAG was detected in maternal peripheral blood at Day 22 of pregnancy (mean +/- SD, 0.38 +/- 0.13 ng/ml) in some animals and at Day 30 in all pregnant cows. Peripheral serum bPAG levels increased progressively to 3.60 +/- 1.73 ng/ml (mean +/- SD) at Day 30 of pregnancy, to 24.53 +/- 8.81 ng/ml at Day 120, and to 1551.91 +/- 589.68 ng/ml at Day 270. Peak concentration of bPAG was 2462.42 +/- 1017.88 ng/ml and it occurred 1-5 days prior to parturition. After delivery, bPAG concentrations decreased steadily to 499.63 +/- 267.20 ng/ml at Day 14 postpartum (pp), 10.12 +/- 7.84 ng/ml at Day 60 pp, and 1.44 +/- 1.08 ng/ml at Day 90 pp. The undetectable concentration (less than 0.20 ng/ml) was reached by Day 100 +/- 20 pp. An investigation undertaken in Holstein heifers, Holstein cows, and Hereford cows used as recipients for purebred Holstein embryos supplied evidence of the influence of breed of recipient and sex of fetuses on peripheral concentrations of bPAG. A herd of 430 Holstein-Friesian heifers that had received transferred embryos were bled at Day 35 postestrus (pe) for measurement of bPAG. The bPAG was detected in 287 of 430 serum samples analyzed. By rectal palpation performed at Day 45 pe, 267 heifers with detectable levels of bPAG at Day 35 pe were confirmed to be pregnant as were 3 of 143 heifers previously diagnosed as not pregnant by RIA. These results suggest that detection of this placental-specific antigen in the serum could be used as a specific serological method for early pregnancy diagnosis in cattle from 28 days after breeding. [less ▲]

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See detailIdentification of the major pregnancy-specific antigens of cattle and sheep as inactive members of the aspartic proteinase family
Xie, Sancai; Low, Boon G.; Nagel, Robert J. et al

in Proceedings of the National Academy of Sciences of the United States of America (1991), 88(22), 10247-10251

Pregnancy in cattle and sheep can be diagnosed by the presence of a conceptus-derived antigen in maternal serum that is secreted by trophoblast and placental tissue primarily as an acidic component of Mr ... [more ▼]

Pregnancy in cattle and sheep can be diagnosed by the presence of a conceptus-derived antigen in maternal serum that is secreted by trophoblast and placental tissue primarily as an acidic component of Mr 67,000. Molecular cloning of its cDNA reveals that the antigen belongs to the aspartic proteinase family and has greater than 50% amino acid sequence identity to pepsin, cathepsin D, and cathepsin E. The inferred sequences of the ovine and bovine polypeptides show approximately 73% identity to each other. Critical amino acid substitutions at the active site regions suggest that both proteins are enzymatically inactive. The antigen is a product of trophoblast binucleate cells that invade maternal endometrium at implantation sites. [less ▲]

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See detailPurification and characterization of a bovine pregnancy-associated glycoprotein
Zoli, André Pagnah; Beckers, Jean-François ULg; Wouters-Ballman, Patricia et al

in Biology of Reproduction (1991), 45(1), 1-10

A 67000 Mr bovine pregnancy-associated glycoprotein (bPAG) has been isolated from fetal cotyledons and purified to homogeneity by HPLC. The purification was monitored by a double immunodiffusion test and ... [more ▼]

A 67000 Mr bovine pregnancy-associated glycoprotein (bPAG) has been isolated from fetal cotyledons and purified to homogeneity by HPLC. The purification was monitored by a double immunodiffusion test and by RIA in conjunction with an antiserum raised against a crude fraction of placenta-specific antigens. The molecular weight of bPAG was estimated to be 67000 by SDS-PAGE. The isoelectric points (pI) of the four isoforms, determined by high-resolution analytical electrofocusing in polyacrylamide gel, were 4.4, 4.6, 5.2, and 5.4. The carbohydrate content of the bPAG consisted of approximately 10.02 +/- 1.09% neutral sugar and variant amounts of sialic acid (from 0.29 +/- 0.06% in the most basic isoform to 2.1 +/- 0.31% in the most acidic isoform). A specific antiserum was raised against the purified bPAG. A specific RIA showed that the bPAG was antigenically unrelated to BSA, alphafetoprotein (AFP), and human schwangerschafts-spezifischen (pregnancy-specific) beta 1 glycoprotein (SP1). According to some characteristics (e.g. the molecular weight), the purified bPAG may correspond to a form of the pregnancy-specific protein B previously described by Sasser and colleagues (Biol Reprod 1986; 35:936-942). [less ▲]

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